Download Class 2 Transferases X: EC 2.7.1.113 - 2.7.5.7 (Springer by Dietmar Schomburg, A. Chang, Ida Schomburg PDF

By Dietmar Schomburg, A. Chang, Ida Schomburg

ISBN-10: 3540478167

ISBN-13: 9783540478164

The target of the Springer guide of Enzymes is to supply in concise shape facts on enzymes sufficiently good characterised. information sheets are prepared of their EC-Number series. The volumes are prepared in line with enzyme sessions. substantial development has been made in enzymology because the booklet of the 1st variation (published as "Enzyme Handbook"): many enzymes are newly categorized or reclassified. within the 2d variation every one access is correlated with references and a number of resource organisms. New datafields are created: "application" and "engineering" (for the houses of enzymes the place the series has been changed). Altogether the volume of information has doubled in order that the second version will encompass 39 volumes plus synonym index. This assortment is an critical resource of data for researchers in biochemistry, biotechnology, natural and analytical chemistry, and nutrition sciences.

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Extra info for Class 2 Transferases X: EC 2.7.1.113 - 2.7.5.7 (Springer Handbook of Enzymes)

Example text

1> [46]) [46] P ADP + ? S ATP + KKRAARATSNVFA <1> (Reversibility: ? <1> [46]) [46] P ADP + ? S ATP + Lys-Lys-Arg-Ala-Ala-Arg-Ala-Thr-Ser-Asn-Val-Phe-Ala <2> (Reversibility: ? <2> [17]) [17] P ADP + ? S ATP + Lys-Lys-Arg-Pro-Gln-Arg-Ala-Thr-Ser-Asn-Val-Phe-Ser <2> (Reversibility: ? <2> [28]) [28] P ADP + ? S ATP + kemptamide <8> (Reversibility: ? <8> [11]) [11] P ADP + ? 5 kDa Dictyostelium or 19 kDa skeletal muscle light chain [20]; <1-3, 5-8, 12> specific for 20 kDa light chain [1, 2, 6, 7, 9, 11, 15, 16, 18-21, 25, 30]; <1-3, 5, 6, 8, 10, 11> not specific for 22 kDa and 15 kDa light chain [2, 33]; <3, 4, 8> not 16 kDa light chain [7, 19, 24]; <2, 3, 5, 6, 8, 10, 11> kinase from skeletal muscle with broader specificity than smooth muscle kinase [33]; <1-3, 5-8> acceptor substrates are myosin light chains of cardiac muscle [2, 9, 10, 18-21]; <1-3, 5-8, 10, 11> acceptor substrates are myosin light chains of skeletal muscle [1-3, 7, 9, 11, 18-21, 33]; <1-3, 5, 6, 8, 10, 11> acceptor substrates are myosin light chains of smooth muscle [2, 5, 6, 9, 11, 12, 21, 23, 28, 30, 33]; <8> acceptor substrates are myosin light chains of adrenal medullary myosin [7]; <1> acceptor substrates are myosin light chains of Ml3-myosin rabbit muscle [1]; <2, 3, 5, 6, 8, 10, 11> acceptor 35 Myosin-light-chain kinase P S P S P S P substrates are myosin light chains of non-muscle myosin [33]; <1-3, 6, 8> acceptor substrates are myosin light chains of smooth muscle myosin [18, 19, 23, 28-30]; <1, 2, 8, 12> 1 mol phosphate per mol light chain in skeletal muscle [7, 21, 25]; <3> transfers the g-phosphate of ATP to a Ser-residue of myosin light chain [19]; <1, 3, 5-8> phosphorylation sites: Serresidues in smooth and skeletal muscle [20]; <1, 3, 5-8> phosphorylation sites: Thr-residues in smooth muscle and pancreas myosin light chain [11, 16, 20]; <1, 3, 5-8> phosphorylation sites: Ser-19 and Thr-18 in smooth muscle myosin light chain [20]; <1> ITP, GTP, CTP or UTP cannot replace ATP [2]; <1-11> no substrate is phosphorylase b [1, 2, 6, 7, 9, 11, 12, 14, 15, 18, 23, 24, 33]; <1-12> no substrate is casein [1, 2, 6, 9, 11, 12, 14, 15, 18, 23-25, 33]; <1-3, 5, 6, 8, 10, 11> no substrate is troponin [1, 2, 33]; <1> no substrates are 15 kDa and 22 kDa light-chain or heavy-chain fractions of myosin from white skeletal muscle [2]; <2-8, 10, 11> no substrates are myosin heavy chain and phosvitin [6, 9, 15, 24, 33]; <12> no substrates are actin and tropomyosin [25]; <6, 7> no substrate is protamine [6, 15]; <1> no substrate is histone III-S from thymus [2]; <2-6, 8, 9, 12> no substrate is histone 2-A [6, 9, 12, 14, 16, 18, 24, 25]; <8, 12> no substrate is histone 2 b [11, 25]; <2, 3, 6, 8> no substrate is histone V-S [6, 12, 18]; <12> no substrate is histone H1 [25]; <2, 3, 5-8, 10, 11> no substrate is phosphorylase kinase [9, 15, 18, 33]; <1> no substrate is molluscan adductor myosin [2, 33]; <5, 8> no substrate is synapsin [11, 16]; <8> no substrates are myelin basic protein, glycogen synthase, tubulin, microtubule-associated protein 2, kemptide and peptide pp60src [11]) (Reversibility: ?

J. Gen. : Thymidine phosphotransferase and nucleotide phosphohydrolase of the fern Asplenium nidus. General properties and inhibition by adenosine 3:5-cyclic monophosphate. Biochem. : Inhibition of the Herpes simplex viruscoded thymidine kinase-complex by 9-b-d-arabinofuranosyladenine 5monophosphate (ara-AMP) and 9-(2-hydroxyethoxymethyl)guanine-monophosphate (acyclo-GMP). Arch. 115 (Protein kinases are in a state of review by the NC-IUBMB. 4 [1-15, 17, 18, 24, 26]; <1,2> branched-chain amino acid metabolism [11, 24]; <3, 2> regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex [15, 24]) (Reversibility: ?

Regulation of the activity of branched-chain 2-oxo acid dehydrogenase (BCODH) complex by binding BCODH kinase. : Branched-chain aketo acid dehydrogenase kinase. : Dietary control and tissue specific expression of branched-chain a-ketoacid dehydrogenase kinase. Arch. Biochem. 116 (Protein kinases are in a state of review by the NC-IUBMB. 116 [Isocitrate dehydrogenase (NADP+)] kinase Natural substrates and products S ATP + [isocitrate dehydrogenase (NADP+ )] <1, 2> (<1, 2> reversible phosphorylation of isocitrate dehydrogenase plays a major role in the control of the Krebs cycle and glyoxylate pathways [1, 5, 6]; <1> phosphorylation of isocitrate dehydrogenase during growth on acetate is to render this enzyme rate-limiting in the citric acid cycle, this should cause an increase in the level of isocitrate and divert the flux of carbon through the glyoxylate bypass [3, 13]; <1> controls the oxidative metabolism, exibits a high intrinsic ATPase activity [9]) (Reversibility: ?

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Class 2 Transferases X: EC 2.7.1.113 - 2.7.5.7 (Springer Handbook of Enzymes) by Dietmar Schomburg, A. Chang, Ida Schomburg


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